GALE_NEIMA
ID GALE_NEIMA Reviewed; 339 AA.
AC P56997; A1IP58;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=UDP-glucose 4-epimerase;
DE EC=5.1.3.2;
DE AltName: Full=Galactowaldenase;
DE AltName: Full=UDP-galactose 4-epimerase;
GN Name=galE; OrderedLocusNames=NMA0203;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
CC -!- FUNCTION: Involved in the metabolism of galactose. Plays an essential
CC role in the incorporation of galactose into meningococcal
CC lipopolysaccharide surface molecules, which are important for
CC pathogenesis. Catalyzes the conversion of UDP-galactose (UDP-Gal) to
CC UDP-glucose (UDP-Glc) through a mechanism involving the transient
CC reduction of NAD (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC EC=5.1.3.2;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AL157959; CAM07517.1; -; Genomic_DNA.
DR PIR; F82014; F82014.
DR RefSeq; WP_002249820.1; NC_003116.1.
DR AlphaFoldDB; P56997; -.
DR SMR; P56997; -.
DR EnsemblBacteria; CAM07517; CAM07517; NMA0203.
DR KEGG; nma:NMA0203; -.
DR HOGENOM; CLU_007383_1_10_4; -.
DR OMA; GEHLICN; -.
DR BioCyc; NMEN122587:NMA_RS01045-MON; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000000626; Chromosome.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01179; galE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Galactose metabolism; Isomerase; NAD.
FT CHAIN 1..339
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000183212"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 32..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 59..60
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217..219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 293..296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 339 AA; 37066 MW; A68DB884417B0C1C CRC64;
MKNILVTGGT GFIGSHTVVS LLKSGHQVVI LDNLCNSSIN ILPRLKTITG QEIPFYQGDI
RDREILRRIF AENRIDSVIH FAGLKAVGES VAEPMKYYDN NVSGSLVLAE EMARAGVFSI
VFSSSATVYG DPGKVPYTED MPLGDTTSPY GTSKSMVERI LTDIQKADPR WSMILLRYFN
PIGAHESGLI GEQPNGIPNN LLPYICQVAS GRLPQLSVFG GDYPTPDGTG MRDYIHVMDL
AEGHVAAMQA KSNVAGTHLL NLGSGRASSV LEIIRAFEAA SGLTIPYEVK PRRAGDLACF
YADPSYTKAQ IGWQTQRDLA QMMEDSWRWV SNNPNGYDD
